Linked Life Data

1477986

Source:http://linkedlifedata.com/resource/pubmed/id/1477986

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1993-2-8
pubmed:abstractText
Reversed-phase HPLC on C18 silica gel at pH 3.5 was used to separate peptides in fraction 9, a mixture of peptides of unknown composition obtained from an enzymic digest of wheat gliadin. This fraction, which has been shown to be toxic to individuals with coeliac disease, yielded a principal peak as well as many minor peaks after HPLC. The significant peaks were subjected to amino acid analysis. The principal peak obtained was purified by rechromatography at pH 6.0 and shown to contain a dodecapeptide of sequence H-Arg-Pro-Gln-Gln-Pro-Tyr-Pro-Gln-Pro-Gln-Pro-Gln-OH. This peptide may have been derived from regions in the A-gliadin molecule corresponding to amino acids numbered 75-86 or from homologous regions in other gliadin molecules. Preliminary results indicate that it is active in two in vitro models of coeliac disease and that it could be the source of one of the undigested peptides (Hexapeptide II, (Glx)3, (Pro)2, Tyr) obtained from coeliac mucosal digestion of fraction 9. Some active serine-containing peptides were also obtained from chromatography at pH 3.5 and attempts are being made to correlate these with the other undigested peptide (Hexapeptide I) of composition (Glx)3, (Pro)2, Ser, obtained after coeliac mucosal digestion of fraction 9.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
213
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-50
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Characterization of the gliadin-derived peptides which are biologically active in coeliac disease.
pubmed:affiliation
Department of Applied Chemistry, Royal Melbourne Institute of Technology, Australia.
pubmed:publicationType
Journal Article